ID   MPPB_BLAEM              Reviewed;         465 AA.
AC   Q00302;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Mitochondrial-processing peptidase subunit beta;
DE            EC=3.4.24.64 {ECO:0000250|UniProtKB:P10507};
DE   AltName: Full=BeMPP1;
DE   AltName: Full=Beta-MPP;
DE   Flags: Precursor;
GN   Name=MPP1;
OS   Blastocladiella emersonii (Aquatic fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Blastocladiella.
OX   NCBI_TaxID=4808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9683495; DOI=10.1128/jb.180.15.3967-3972.1998;
RA   Costa-Rocha C.R., Lopes-Gomes S.;
RT   "Isolation, characterization, and expression of the gene encoding the beta
RT   subunit of the mitochondrial processing peptidase from Blastocladiella
RT   emersonii.";
RL   J. Bacteriol. 180:3967-3972(1998).
CC   -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC       protease (MPP), which cleaves the mitochondrial sequence off newly
CC       imported precursors proteins (By similarity). Preferentially, cleaves
CC       after an arginine at position P2 (By similarity).
CC       {ECO:0000250|UniProtKB:P10507, ECO:0000250|UniProtKB:Q03346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal transit peptides from precursor proteins
CC         imported into the mitochondrion, typically with Arg in position P2.;
CC         EC=3.4.24.64; Evidence={ECO:0000250|UniProtKB:P10507};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P10507};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
CC   -!- ACTIVITY REGULATION: Binding to the alpha subunit is required for
CC       catalytic activity. {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit subunits,
CC       forming the mitochondrial processing protease (MPP) in which the alpha
CC       subunit is involved in substrate recognition and binding and the beta
CC       subunit is the catalytic subunit. {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P10507}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; U41300; AAC63093.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00302; -.
DR   SMR; Q00302; -.
DR   MEROPS; M16.980; -.
DR   PRIDE; Q00302; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Transit peptide; Zinc.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..465
FT                   /note="Mitochondrial-processing peptidase subunit beta"
FT                   /id="PRO_0000026780"
FT   ACT_SITE        82
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10507"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10507"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10507"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10507"
SQ   SEQUENCE   465 AA;  50683 MW;  CA38C439E1DA9AB2 CRC64;
     MLSAALRLTA KRNVRSLATA SSSSYPGALL NVPKTQVTRL PNGLTVATES NPALATATVG
     VWIDSGSRAE TKANNGVAHF LEHISFKGTK QRTQSGLEIE IENMGGHLNA YTSREQTVYY
     AKLFSQDVAK GVNILGDILQ NSTLDPGAID RERAVILREA EEVDKQVEEV VFDHLHAAAF
     PENALGYTIL GPKENIQTLS QADLQAYIKN NYTADRMVVV GAGNVDHAEL CKLAETNFGK
     LPQGSGKAKF VRPAFTGSDV RIRVDDMPTA HIALAVEGAS WTSADHWPLL VASAMIGSYD
     RAAGNAHPSS KLAQIVAKHN LANSFTSFNT TYSDTGLWGI YIQSNNRDNL DDLAHFTVRE
     WMRLATAPSE GEVAIAKQQL KTSLLLALDG TTPVAEEIGR QMLAYGRRLS PFEIDRLVDA
     VTVEDVKRVA NEFIYDRDLA IVAVGPVECL PDYNRIRSAM NLLRY